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J Cell Sci. 2017 Jan 15;130(2):480-489. doi: 10.1242/jcs.195503. Epub 2016 Dec 1.

Heterochromatin aggregation during DNA elimination in Tetrahymena is facilitated by a prion-like protein.

Author information

1
Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Dr Bohr-Gasse 3, Vienna A-1030, Austria.
2
Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Dr Bohr-Gasse 3, Vienna A-1030, Austria kazufumi.mochizuki@igh.cnrs.fr.
3
Institute of Human Genetics (IGH), CNRS UPR1142, 141 rue de la Cardonille, Montpellier Cedex 5 34396, France.

Abstract

Regulated aggregations of prion and prion-like proteins play physiological roles in various biological processes. However, their structural roles in the nucleus are poorly understood. Here, we show that the prion-like protein Jub6p is involved in the regulation of chromatin structure in the ciliated protozoan Tetrahymena thermophila Jub6p forms sodium dodecyl sulfate (SDS)-resistant aggregates when it is ectopically expressed in vegetative cells and binds to RNA in vitro Jub6p is a heterochromatin component and is important for the formation of heterochromatin bodies during the process of programmed DNA elimination. We suggest that RNA-protein aggregates formed by Jub6p are an essential architectural component for the assembly of heterochromatin bodies.

KEYWORDS:

DNA elimination; Heterochromatin; Heterochromatin body; Prion; Tetrahymena

PMID:
27909245
DOI:
10.1242/jcs.195503
[Indexed for MEDLINE]
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